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Volumn 3, Issue 3-4, 2012, Pages 274-282

The Roles of MDM2 and MDMX Phosphorylation in Stress Signaling to p53

Author keywords

MDM2; MDMX; p53; phosphorylation; ubiquitination

Indexed keywords

ABELSON KINASE; ARF PROTEIN; ATM PROTEIN; CASEIN KINASE IALPHA; CHECKPOINT KINASE 2; DNA; PROTEIN MDM2; PROTEIN MDMX; PROTEIN P53; RIBOSOME PROTEIN; UBIQUITIN PROTEIN LIGASE E3;

EID: 84875535434     PISSN: 19476019     EISSN: 19476027     Source Type: Journal    
DOI: 10.1177/1947601912454733     Document Type: Article
Times cited : (27)

References (126)
  • 3
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt Y,Maya R,Kazaz A,Oren M.Mdm2 promotes the rapid degradation of p53.Nature. 1997;387:296-9.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 4
    • 0037459377 scopus 로고    scopus 로고
    • Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation
    • Leng RP,Lin Y,Ma W, et al.Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation.Cell. 2003;112:779-91.
    • (2003) Cell , vol.112 , pp. 779-791
    • Leng, R.P.1    Lin, Y.2    Ma, W.3
  • 5
    • 2342447397 scopus 로고    scopus 로고
    • The ubiquitin ligase COP1 is a critical negative regulator of p53
    • Dornan D,Wertz I,Shimizu H, et al.The ubiquitin ligase COP1 is a critical negative regulator of p53.Nature. 2004;429:86-92.
    • (2004) Nature , vol.429 , pp. 86-92
    • Dornan, D.1    Wertz, I.2    Shimizu, H.3
  • 6
    • 0028823020 scopus 로고
    • Rescue of early embryonic lethality in Mdm2-deficient mice by deletion of p53
    • Montes de Oca Luna R,Wagner DS,Lozano G.Rescue of early embryonic lethality in Mdm2-deficient mice by deletion of p53.Nature. 1995;378:203-6.
    • (1995) Nature , vol.378 , pp. 203-206
    • Montes de Oca Luna, R.1    Wagner, D.S.2    Lozano, G.3
  • 8
    • 0028834902 scopus 로고
    • Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53
    • Jones SN,Roe AE,Donehower LA,Bradley A.Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53.Nature. 1995;378:206-8.
    • (1995) Nature , vol.378 , pp. 206-208
    • Jones, S.N.1    Roe, A.E.2    Donehower, L.A.3    Bradley, A.4
  • 9
    • 10744221485 scopus 로고    scopus 로고
    • In vivo activation of the p53 pathway by small-molecule antagonists of MDM2
    • Vassilev LT,Vu BT,Graves B, et al.In vivo activation of the p53 pathway by small-molecule antagonists of MDM2.Science. 2004;303:844-8.
    • (2004) Science , vol.303 , pp. 844-848
    • Vassilev, L.T.1    Vu, B.T.2    Graves, B.3
  • 10
    • 41649102468 scopus 로고    scopus 로고
    • Temporal activation of p53 by a specific MDM2 inhibitor is selectively toxic to tumors and leads to complete tumor growth inhibition
    • Shangary S,Qin D,McEachern D, et al.Temporal activation of p53 by a specific MDM2 inhibitor is selectively toxic to tumors and leads to complete tumor growth inhibition.Proc Natl Acad Sci U S A. 2008;105:3933-8.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 3933-3938
    • Shangary, S.1    Qin, D.2    McEachern, D.3
  • 11
    • 10144259344 scopus 로고    scopus 로고
    • MDMX: a novel p53-binding protein with some functional properties of MDM2
    • Shvarts A,Steegenga WT,Riteco N, et al.MDMX: a novel p53-binding protein with some functional properties of MDM2.EMBO J. 1996;15:5349-57.
    • (1996) EMBO J , vol.15 , pp. 5349-5357
    • Shvarts, A.1    Steegenga, W.T.2    Riteco, N.3
  • 12
    • 0036606416 scopus 로고    scopus 로고
    • Mdmx is a negative regulator of p53 activity in vivo
    • Finch RA,Donoviel DB,Potter D, et al.Mdmx is a negative regulator of p53 activity in vivo.Cancer Res. 2002;62:3221-5.
    • (2002) Cancer Res , vol.62 , pp. 3221-3225
    • Finch, R.A.1    Donoviel, D.B.2    Potter, D.3
  • 13
    • 0036311067 scopus 로고    scopus 로고
    • Mdm4 (Mdmx) regulates p53-induced growth arrest and neuronal cell death during early embryonic mouse development
    • Migliorini D,Lazzerini Denchi E,Danovi D, et al.Mdm4 (Mdmx) regulates p53-induced growth arrest and neuronal cell death during early embryonic mouse development.Mol Cell Biol. 2002;22:5527-38.
    • (2002) Mol Cell Biol , vol.22 , pp. 5527-5538
    • Migliorini, D.1    Lazzerini Denchi, E.2    Danovi, D.3
  • 14
    • 0035972822 scopus 로고    scopus 로고
    • Organization, expression, and localization of the murine Mdmx gene and pseudogene
    • Parant JM,Reinke V,Mims B,Lozano G.Organization, expression, and localization of the murine Mdmx gene and pseudogene.Gene. 2001;270:277-83.
    • (2001) Gene , vol.270 , pp. 277-283
    • Parant, J.M.1    Reinke, V.2    Mims, B.3    Lozano, G.4
  • 16
    • 33947250363 scopus 로고    scopus 로고
    • Distinct roles of Mdm2 and Mdm4 in red cell production
    • Maetens M,Doumont G,Clercq SD, et al.Distinct roles of Mdm2 and Mdm4 in red cell production.Blood. 2007;109:2630-3.
    • (2007) Blood , vol.109 , pp. 2630-2633
    • Maetens, M.1    Doumont, G.2    Clercq, S.D.3
  • 17
    • 28344454072 scopus 로고    scopus 로고
    • Rescue of Mdm4-deficient mice by Mdm2 reveals functional overlap of Mdm2 and Mdm4 in development
    • Steinman HA,Hoover KM,Keeler ML,Sands AT,Jones SN.Rescue of Mdm4-deficient mice by Mdm2 reveals functional overlap of Mdm2 and Mdm4 in development.Oncogene. 2005;24:7935-40.
    • (2005) Oncogene , vol.24 , pp. 7935-7940
    • Steinman, H.A.1    Hoover, K.M.2    Keeler, M.L.3    Sands, A.T.4    Jones, S.N.5
  • 18
    • 77953571903 scopus 로고    scopus 로고
    • p53 inactivation by MDM2 and MDMX negative feedback loops in testicular germ cell tumors
    • Li B,Cheng Q,Li Z,Chen J.p53 inactivation by MDM2 and MDMX negative feedback loops in testicular germ cell tumors.Cell Cycle. 2010;9:1411-20.
    • (2010) Cell Cycle , vol.9 , pp. 1411-1420
    • Li, B.1    Cheng, Q.2    Li, Z.3    Chen, J.4
  • 19
    • 77956518104 scopus 로고    scopus 로고
    • HDMX-L is expressed from a functional p53-responsive promoter in the first intron of the HDMX gene and participates in an autoregulatory feedback loop to control p53 activity
    • Phillips A,Teunisse A,Lam S, et al.HDMX-L is expressed from a functional p53-responsive promoter in the first intron of the HDMX gene and participates in an autoregulatory feedback loop to control p53 activity.J Biol Chem. 2010;285:29111-27.
    • (2010) J Biol Chem , vol.285 , pp. 29111-29127
    • Phillips, A.1    Teunisse, A.2    Lam, S.3
  • 20
    • 0034708458 scopus 로고    scopus 로고
    • Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53
    • Fang S,Jensen JP,Ludwig RL,Vousden KH,Weissman AM.Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53.J Biol Chem. 2000;275:8945-51.
    • (2000) J Biol Chem , vol.275 , pp. 8945-8951
    • Fang, S.1    Jensen, J.P.2    Ludwig, R.L.3    Vousden, K.H.4    Weissman, A.M.5
  • 21
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
    • Honda R,Tanaka H,Yasuda H.Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53.FEBS Lett. 1997;420:25-7.
    • (1997) FEBS Lett , vol.420 , pp. 25-27
    • Honda, R.1    Tanaka, H.2    Yasuda, H.3
  • 22
    • 28444437051 scopus 로고    scopus 로고
    • MDM2 promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma protein
    • Sdek P,Ying H,Chang DL, et al.MDM2 promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma protein.Mol Cell. 2005;20:699-708.
    • (2005) Mol Cell , vol.20 , pp. 699-708
    • Sdek, P.1    Ying, H.2    Chang, D.L.3
  • 23
    • 0038788827 scopus 로고    scopus 로고
    • Critical contribution of the MDM2 acidic domain to p53 ubiquitination
    • Kawai H,Wiederschain D,Yuan ZM.Critical contribution of the MDM2 acidic domain to p53 ubiquitination.Mol Cell Biol. 2003;23:4939-47.
    • (2003) Mol Cell Biol , vol.23 , pp. 4939-4947
    • Kawai, H.1    Wiederschain, D.2    Yuan, Z.M.3
  • 24
    • 0038451241 scopus 로고    scopus 로고
    • Critical role for a central part of Mdm2 in the ubiquitylation of p53
    • Meulmeester E,Frenk R,Stad R, et al.Critical role for a central part of Mdm2 in the ubiquitylation of p53.Mol Cell Biol. 2003;23:4929-38.
    • (2003) Mol Cell Biol , vol.23 , pp. 4929-4938
    • Meulmeester, E.1    Frenk, R.2    Stad, R.3
  • 25
    • 25144496653 scopus 로고    scopus 로고
    • MDM2 interaction with nuclear corepressor KAP1 contributes to p53 inactivation
    • Wang C,Ivanov A,Chen L, et al.MDM2 interaction with nuclear corepressor KAP1 contributes to p53 inactivation.EMBO J. 2005;24:3279-90.
    • (2005) EMBO J , vol.24 , pp. 3279-3290
    • Wang, C.1    Ivanov, A.2    Chen, L.3
  • 26
    • 2942702012 scopus 로고    scopus 로고
    • Yin Yang 1 is a negative regulator of p53
    • Sui G,Affar el B,Shi Y, et al.Yin Yang 1 is a negative regulator of p53.Cell. 2004;117:859-72.
    • (2004) Cell , vol.117 , pp. 859-872
    • Sui, G.1    Affar el, B.2    Shi, Y.3
  • 27
    • 77955415488 scopus 로고    scopus 로고
    • MDM2 recruitment of lysine methyltransferases regulates p53 transcriptional output
    • Chen L,Li Z,Zwolinska AK, et al.MDM2 recruitment of lysine methyltransferases regulates p53 transcriptional output.EMBO J. 2010;29:2538-52.
    • (2010) EMBO J , vol.29 , pp. 2538-2552
    • Chen, L.1    Li, Z.2    Zwolinska, A.K.3
  • 28
    • 33244490784 scopus 로고    scopus 로고
    • Structural basis of competitive recognition of p53 and MDM2 by HAUSP/USP7: implications for the regulation of the p53-MDM2 pathway
    • Hu M,Gu L,Li M,Jeffrey PD,Gu W,Shi Y.Structural basis of competitive recognition of p53 and MDM2 by HAUSP/USP7: implications for the regulation of the p53-MDM2 pathway.PLoS Biol. 2006;4:e27.
    • (2006) PLoS Biol , vol.4
    • Hu, M.1    Gu, L.2    Li, M.3    Jeffrey, P.D.4    Gu, W.5    Shi, Y.6
  • 29
    • 0242721592 scopus 로고    scopus 로고
    • Ribosomal protein L11 negatively regulates oncoprotein MDM2 and mediates a p53-dependent ribosomal-stress checkpoint pathway
    • Zhang Y,Wolf GW,Bhat K, et al.Ribosomal protein L11 negatively regulates oncoprotein MDM2 and mediates a p53-dependent ribosomal-stress checkpoint pathway.Mol Cell Biol. 2003;23:8902-12.
    • (2003) Mol Cell Biol , vol.23 , pp. 8902-8912
    • Zhang, Y.1    Wolf, G.W.2    Bhat, K.3
  • 30
    • 0034603897 scopus 로고    scopus 로고
    • An N-terminal p14ARF peptide blocks Mdm2-dependent ubiquitination in vitro and can activate p53 in vivo
    • Midgley CA,Desterro JM,Saville MK, et al.An N-terminal p14ARF peptide blocks Mdm2-dependent ubiquitination in vitro and can activate p53 in vivo.Oncogene. 2000;19:2312-23.
    • (2000) Oncogene , vol.19 , pp. 2312-2323
    • Midgley, C.A.1    Desterro, J.M.2    Saville, M.K.3
  • 31
    • 33746642476 scopus 로고    scopus 로고
    • A second p53 binding site in the central domain of Mdm2 is essential for p53 ubiquitination
    • Ma J,Martin JD,Zhang H, et al.A second p53 binding site in the central domain of Mdm2 is essential for p53 ubiquitination.Biochemistry. 2006;45:9238-45.
    • (2006) Biochemistry , vol.45 , pp. 9238-9245
    • Ma, J.1    Martin, J.D.2    Zhang, H.3
  • 33
    • 0034697107 scopus 로고    scopus 로고
    • Mdm2 binding to a conformationally sensitive domain on p53 can be modulated by RNA
    • Burch LR,Midgley CA,Currie RA,Lane DP,Hupp TR.Mdm2 binding to a conformationally sensitive domain on p53 can be modulated by RNA.FEBS Lett. 2000;472:93-8.
    • (2000) FEBS Lett , vol.472 , pp. 93-98
    • Burch, L.R.1    Midgley, C.A.2    Currie, R.A.3    Lane, D.P.4    Hupp, T.R.5
  • 34
    • 79955534071 scopus 로고    scopus 로고
    • Inhibition of p53 DNA binding function by the MDM2 protein acidic domain
    • Cross B,Chen L,Cheng Q,Li B,Yuan ZM,Chen J.Inhibition of p53 DNA binding function by the MDM2 protein acidic domain.J Biol Chem. 2011;286:16018-29.
    • (2011) J Biol Chem , vol.286 , pp. 16018-16029
    • Cross, B.1    Chen, L.2    Cheng, Q.3    Li, B.4    Yuan, Z.M.5    Chen, J.6
  • 35
    • 34347205250 scopus 로고    scopus 로고
    • MDM2 binding induces a conformational change in p53 that is opposed by heat-shock protein 90 and precedes p53 proteasomal degradation
    • Sasaki M,Nie L,Maki CG.MDM2 binding induces a conformational change in p53 that is opposed by heat-shock protein 90 and precedes p53 proteasomal degradation.J Biol Chem. 2007;282:14626-34.
    • (2007) J Biol Chem , vol.282 , pp. 14626-14634
    • Sasaki, M.1    Nie, L.2    Maki, C.G.3
  • 37
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson HJ,Wright PE.Intrinsically unstructured proteins and their functions.Nat Rev Mol Cell Biol. 2005;6:197-208.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 38
    • 0037147143 scopus 로고    scopus 로고
    • MdmX is a RING finger ubiquitin ligase capable of synergistically enhancing Mdm2 ubiquitination
    • Badciong JC,Haas AL.MdmX is a RING finger ubiquitin ligase capable of synergistically enhancing Mdm2 ubiquitination.J Biol Chem. 2002;277:49668-75.
    • (2002) J Biol Chem , vol.277 , pp. 49668-49675
    • Badciong, J.C.1    Haas, A.L.2
  • 39
    • 33644778697 scopus 로고    scopus 로고
    • Mdm4 and Mdm2 cooperate to inhibit p53 activity in proliferating and quiescent cells in vivo
    • Francoz S,Froment P,Bogaerts S, et al.Mdm4 and Mdm2 cooperate to inhibit p53 activity in proliferating and quiescent cells in vivo.Proc Natl Acad Sci U S A. 2006;103:3232-7.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 3232-3237
    • Francoz, S.1    Froment, P.2    Bogaerts, S.3
  • 40
    • 33751573462 scopus 로고    scopus 로고
    • MDMX regulation of p53 response to ribosomal stress
    • Gilkes DM,Chen L,Chen J.MDMX regulation of p53 response to ribosomal stress.EMBO J. 2006;25:5614-25.
    • (2006) EMBO J , vol.25 , pp. 5614-5625
    • Gilkes, D.M.1    Chen, L.2    Chen, J.3
  • 41
    • 33645769536 scopus 로고    scopus 로고
    • A mouse p53 mutant lacking the proline-rich domain rescues Mdm4 deficiency and provides insight into the Mdm2-Mdm4-p53 regulatory network
    • Toledo F,Krummel KA,Lee CJ, et al.A mouse p53 mutant lacking the proline-rich domain rescues Mdm4 deficiency and provides insight into the Mdm2-Mdm4-p53 regulatory network.Cancer Cell. 2006;9:273-85.
    • (2006) Cancer Cell , vol.9 , pp. 273-285
    • Toledo, F.1    Krummel, K.A.2    Lee, C.J.3
  • 42
    • 0042592947 scopus 로고    scopus 로고
    • MDM2 promotes ubiquitination and degradation of MDMX
    • Pan Y,Chen J.MDM2 promotes ubiquitination and degradation of MDMX.Mol Cell Biol. 2003;23:5113-21.
    • (2003) Mol Cell Biol , vol.23 , pp. 5113-5121
    • Pan, Y.1    Chen, J.2
  • 43
    • 42149105590 scopus 로고    scopus 로고
    • Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans
    • Linke K,Mace PD,Smith CA,Vaux DL,Silke J,Day CL.Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans.Cell Death Differ. 2008;15:841-8.
    • (2008) Cell Death Differ , vol.15 , pp. 841-848
    • Linke, K.1    Mace, P.D.2    Smith, C.A.3    Vaux, D.L.4    Silke, J.5    Day, C.L.6
  • 44
    • 33846193699 scopus 로고    scopus 로고
    • An essential function of the extreme C-terminus of MDM2 can be provided by MDMX
    • Uldrijan S,Pannekoek WJ,Vousden KH.An essential function of the extreme C-terminus of MDM2 can be provided by MDMX.EMBO J. 2007;26:102-12.
    • (2007) EMBO J , vol.26 , pp. 102-112
    • Uldrijan, S.1    Pannekoek, W.J.2    Vousden, K.H.3
  • 47
    • 0037205454 scopus 로고    scopus 로고
    • Mutual dependence of MDM2 and MDMX in their functional inactivation of p53
    • Gu J,Kawai H,Nie L, et al.Mutual dependence of MDM2 and MDMX in their functional inactivation of p53.J Biol Chem. 2002;277:19251-4.
    • (2002) J Biol Chem , vol.277 , pp. 19251-19254
    • Gu, J.1    Kawai, H.2    Nie, L.3
  • 48
    • 79959881127 scopus 로고    scopus 로고
    • MdmX protein is essential for Mdm2 protein-mediated p53 polyubiquitination
    • Wang X,Wang J,Jiang X.MdmX protein is essential for Mdm2 protein-mediated p53 polyubiquitination.J Biol Chem. 2011;286:23725-34.
    • (2011) J Biol Chem , vol.286 , pp. 23725-23734
    • Wang, X.1    Wang, J.2    Jiang, X.3
  • 49
    • 69249202241 scopus 로고    scopus 로고
    • Mdmx enhances p53 ubiquitination by altering the substrate preference of the Mdm2 ubiquitin ligase
    • Okamoto K,Taya Y,Nakagama H.Mdmx enhances p53 ubiquitination by altering the substrate preference of the Mdm2 ubiquitin ligase.FEBS Lett. 2009;583:2710-4.
    • (2009) FEBS Lett , vol.583 , pp. 2710-2714
    • Okamoto, K.1    Taya, Y.2    Nakagama, H.3
  • 50
    • 34447123808 scopus 로고    scopus 로고
    • RING domain-mediated interaction is a requirement for MDM2's E3 ligase activity
    • Kawai H,Lopez-Pajares V,Kim MM,Wiederschain D,Yuan ZM.RING domain-mediated interaction is a requirement for MDM2's E3 ligase activity.Cancer Res. 2007;67:6026-30.
    • (2007) Cancer Res , vol.67 , pp. 6026-6030
    • Kawai, H.1    Lopez-Pajares, V.2    Kim, M.M.3    Wiederschain, D.4    Yuan, Z.M.5
  • 51
    • 79961076734 scopus 로고    scopus 로고
    • The p53 inhibitors MDM2/MDMX complex is required for control of p53 activity in vivo
    • Huang L,Yan Z,Liao X, et al.The p53 inhibitors MDM2/MDMX complex is required for control of p53 activity in vivo.Proc Natl Acad Sci U S A. 2011;108:12001-6.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 12001-12006
    • Huang, L.1    Yan, Z.2    Liao, X.3
  • 52
    • 33747819484 scopus 로고    scopus 로고
    • Divorcing ARF and p53: an unsettled case
    • Sherr CJ.Divorcing ARF and p53: an unsettled case.Nat Rev Cancer. 2006;6:663-73.
    • (2006) Nat Rev Cancer , vol.6 , pp. 663-673
    • Sherr, C.J.1
  • 53
    • 70350497397 scopus 로고    scopus 로고
    • Signaling to p53: ribosomal proteins find their way
    • Zhang Y,Lu H.Signaling to p53: ribosomal proteins find their way.Cancer Cell. 2009;16:369-77.
    • (2009) Cancer Cell , vol.16 , pp. 369-377
    • Zhang, Y.1    Lu, H.2
  • 54
    • 0026496885 scopus 로고
    • A mammalian cell cycle checkpoint pathway utilizing p53 and GADD45 is defective in ataxia-telangiectasia
    • Kastan MB,Zhan Q,El-Deiry WS, et al.A mammalian cell cycle checkpoint pathway utilizing p53 and GADD45 is defective in ataxia-telangiectasia.Cell. 1992;71:587-97.
    • (1992) Cell , vol.71 , pp. 587-597
    • Kastan, M.B.1    Zhan, Q.2    El-Deiry, W.S.3
  • 55
    • 0037365789 scopus 로고    scopus 로고
    • ATM and related protein kinases: safeguarding genome integrity
    • Shiloh Y.ATM and related protein kinases: safeguarding genome integrity.Nat Rev Cancer. 2003;3:155-68.
    • (2003) Nat Rev Cancer , vol.3 , pp. 155-168
    • Shiloh, Y.1
  • 56
    • 78649336706 scopus 로고    scopus 로고
    • The DNA damage response: making it safe to play with knives
    • Ciccia A,Elledge SJ.The DNA damage response: making it safe to play with knives.Mol Cell. 2010;40:179-204.
    • (2010) Mol Cell , vol.40 , pp. 179-204
    • Ciccia, A.1    Elledge, S.J.2
  • 57
    • 0032508504 scopus 로고    scopus 로고
    • Enhanced phosphorylation of p53 by ATM in response to DNA damage
    • Banin S,Moyal L,Shieh S, et al.Enhanced phosphorylation of p53 by ATM in response to DNA damage.Science. 1998;281:1674-7.
    • (1998) Science , vol.281 , pp. 1674-1677
    • Banin, S.1    Moyal, L.2    Shieh, S.3
  • 58
    • 0030667702 scopus 로고    scopus 로고
    • DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
    • Shieh SY,Ikeda M,Taya Y,Prives C.DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2.Cell. 1997;91:325-34.
    • (1997) Cell , vol.91 , pp. 325-334
    • Shieh, S.Y.1    Ikeda, M.2    Taya, Y.3    Prives, C.4
  • 59
    • 0034142325 scopus 로고    scopus 로고
    • Chk2/hCds1 functions as a DNA damage checkpoint in G(1) by stabilizing p53
    • Chehab NH,Malikzay A,Appel M,Halazonetis TD.Chk2/hCds1 functions as a DNA damage checkpoint in G(1) by stabilizing p53.Genes Dev. 2000;14:278-88.
    • (2000) Genes Dev , vol.14 , pp. 278-288
    • Chehab, N.H.1    Malikzay, A.2    Appel, M.3    Halazonetis, T.D.4
  • 60
    • 0034142034 scopus 로고    scopus 로고
    • The human homologs of checkpoint kinases Chk1 and Cds1 (Chk2) phosphorylate p53 at multiple DNA damage-inducible sites
    • Shieh SY,Ahn J,Tamai K,Taya Y,Prives C.The human homologs of checkpoint kinases Chk1 and Cds1 (Chk2) phosphorylate p53 at multiple DNA damage-inducible sites.Genes Dev. 2000;14:289-300.
    • (2000) Genes Dev , vol.14 , pp. 289-300
    • Shieh, S.Y.1    Ahn, J.2    Tamai, K.3    Taya, Y.4    Prives, C.5
  • 61
    • 0033020147 scopus 로고    scopus 로고
    • Regulation of p53 function and stability by phosphorylation
    • Ashcroft M,Kubbutat MH,Vousden KH.Regulation of p53 function and stability by phosphorylation.Mol Cell Biol. 1999;19:1751-8.
    • (1999) Mol Cell Biol , vol.19 , pp. 1751-1758
    • Ashcroft, M.1    Kubbutat, M.H.2    Vousden, K.H.3
  • 62
    • 0033522143 scopus 로고    scopus 로고
    • DNA damage induced p53 stabilization: no indication for an involvement of p53 phosphorylation
    • Blattner C,Tobiasch E,Litfen M,Rahmsdorf HJ,Herrlich P.DNA damage induced p53 stabilization: no indication for an involvement of p53 phosphorylation.Oncogene. 1999;18:1723-32.
    • (1999) Oncogene , vol.18 , pp. 1723-1732
    • Blattner, C.1    Tobiasch, E.2    Litfen, M.3    Rahmsdorf, H.J.4    Herrlich, P.5
  • 63
    • 0033572746 scopus 로고    scopus 로고
    • Serine15 phosphorylation stimulates p53 transactivation but does not directly influence interaction with HDM2
    • Dumaz N,Meek DW.Serine15 phosphorylation stimulates p53 transactivation but does not directly influence interaction with HDM2.EMBO J. 1999;18:7002-10.
    • (1999) EMBO J , vol.18 , pp. 7002-7010
    • Dumaz, N.1    Meek, D.W.2
  • 64
    • 33745752959 scopus 로고    scopus 로고
    • Ser18 and 23 phosphorylation is required for p53-dependent apoptosis and tumor suppression
    • Chao C,Herr D,Chun J,Xu Y.Ser18 and 23 phosphorylation is required for p53-dependent apoptosis and tumor suppression.EMBO J. 2006;25:2615-22.
    • (2006) EMBO J , vol.25 , pp. 2615-2622
    • Chao, C.1    Herr, D.2    Chun, J.3    Xu, Y.4
  • 65
    • 20844451888 scopus 로고    scopus 로고
    • Defective apoptosis and B-cell lymphomas in mice with p53 point mutation at Ser 23
    • MacPherson D,Kim J,Kim T, et al.Defective apoptosis and B-cell lymphomas in mice with p53 point mutation at Ser 23.EMBO J. 2004;23:3689-99.
    • (2004) EMBO J , vol.23 , pp. 3689-3699
    • MacPherson, D.1    Kim, J.2    Kim, T.3
  • 66
    • 0142039901 scopus 로고    scopus 로고
    • Cell type- and promoter-specific roles of Ser18 phosphorylation in regulating p53 responses
    • Chao C,Hergenhahn M,Kaeser MD, et al.Cell type- and promoter-specific roles of Ser18 phosphorylation in regulating p53 responses.J Biol Chem. 2003;278:41028-33.
    • (2003) J Biol Chem , vol.278 , pp. 41028-41033
    • Chao, C.1    Hergenhahn, M.2    Kaeser, M.D.3
  • 67
    • 0035339357 scopus 로고    scopus 로고
    • ATM-dependent phosphorylation of Mdm2 on serine 395: role in p53 activation by DNA damage
    • Maya R,Balass M,Kim ST, et al.ATM-dependent phosphorylation of Mdm2 on serine 395: role in p53 activation by DNA damage.Genes Dev. 2001;15:1067-77.
    • (2001) Genes Dev , vol.15 , pp. 1067-1077
    • Maya, R.1    Balass, M.2    Kim, S.T.3
  • 68
    • 0347363827 scopus 로고    scopus 로고
    • Functional role of Mdm2 phosphorylation by ATR in attenuation of p53 nuclear export
    • Shinozaki T,Nota A,Taya Y,Okamoto K.Functional role of Mdm2 phosphorylation by ATR in attenuation of p53 nuclear export.Oncogene. 2003;22:8870-80.
    • (2003) Oncogene , vol.22 , pp. 8870-8880
    • Shinozaki, T.1    Nota, A.2    Taya, Y.3    Okamoto, K.4
  • 69
    • 0034898859 scopus 로고    scopus 로고
    • c-Abl regulates p53 levels under normal and stress conditions by preventing its nuclear export and ubiquitination
    • Sionov RV,Coen S,Goldberg Z, et al.c-Abl regulates p53 levels under normal and stress conditions by preventing its nuclear export and ubiquitination.Mol Cell Biol. 2001;21:5869-78.
    • (2001) Mol Cell Biol , vol.21 , pp. 5869-5878
    • Sionov, R.V.1    Coen, S.2    Goldberg, Z.3
  • 70
    • 0037099586 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Mdm2 by c-Abl: implications for p53 regulation
    • Goldberg Z,Vogt Sionov R,Berger M, et al.Tyrosine phosphorylation of Mdm2 by c-Abl: implications for p53 regulation.EMBO J. 2002;21:3715-27.
    • (2002) EMBO J , vol.21 , pp. 3715-3727
    • Goldberg, Z.1    Vogt Sionov, R.2    Berger, M.3
  • 71
    • 72449125109 scopus 로고    scopus 로고
    • ATM activates p53 by regulating MDM2 oligomerization and E3 processivity
    • Cheng Q,Chen L,Li Z,Lane WS,Chen J.ATM activates p53 by regulating MDM2 oligomerization and E3 processivity.EMBO J. 2009;28:3857-67.
    • (2009) EMBO J , vol.28 , pp. 3857-3867
    • Cheng, Q.1    Chen, L.2    Li, Z.3    Lane, W.S.4    Chen, J.5
  • 72
    • 2342473198 scopus 로고    scopus 로고
    • The importance of intrinsic disorder for protein phosphorylation
    • Iakoucheva LM,Radivojac P,Brown CJ, et al.The importance of intrinsic disorder for protein phosphorylation.Nucleic Acids Res. 2004;32:1037-49.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1037-1049
    • Iakoucheva, L.M.1    Radivojac, P.2    Brown, C.J.3
  • 73
    • 83255162746 scopus 로고    scopus 로고
    • Regulation of MDM2 E3 ligase activity by phosphorylation after DNA damage
    • Cheng Q,Cross B,Li B,Chen L,Li Z,Chen J.Regulation of MDM2 E3 ligase activity by phosphorylation after DNA damage.Mol Cell Biol. 2011;31:4951-63.
    • (2011) Mol Cell Biol , vol.31 , pp. 4951-4963
    • Cheng, Q.1    Cross, B.2    Li, B.3    Chen, L.4    Li, Z.5    Chen, J.6
  • 74
    • 80054837173 scopus 로고    scopus 로고
    • Antagonists induce a conformational change in cIAP1 that promotes autoubiquitination
    • Dueber EC,Schoeffler AJ,Lingel A, et al.Antagonists induce a conformational change in cIAP1 that promotes autoubiquitination.Science. 2011;334:376-80.
    • (2011) Science , vol.334 , pp. 376-380
    • Dueber, E.C.1    Schoeffler, A.J.2    Lingel, A.3
  • 76
    • 1642576077 scopus 로고    scopus 로고
    • Dimerization of the human E3 ligase CHIP via a coiled-coil domain is essential for its activity
    • Nikolay R,Wiederkehr T,Rist W,Kramer G,Mayer MP,Bukau B.Dimerization of the human E3 ligase CHIP via a coiled-coil domain is essential for its activity.J Biol Chem. 2004;279:2673-8.
    • (2004) J Biol Chem , vol.279 , pp. 2673-2678
    • Nikolay, R.1    Wiederkehr, T.2    Rist, W.3    Kramer, G.4    Mayer, M.P.5    Bukau, B.6
  • 77
    • 57649120782 scopus 로고    scopus 로고
    • Structures of the cIAP2 RING domain reveal conformational changes associated with ubiquitin-conjugating enzyme (E2) recruitment
    • Mace PD,Linke K,Feltham R, et al.Structures of the cIAP2 RING domain reveal conformational changes associated with ubiquitin-conjugating enzyme (E2) recruitment.J Biol Chem. 2008;283:31633-40.
    • (2008) J Biol Chem , vol.283 , pp. 31633-31640
    • Mace, P.D.1    Linke, K.2    Feltham, R.3
  • 78
    • 30144439025 scopus 로고    scopus 로고
    • The Prp19 U-box crystal structure suggests a common dimeric architecture for a class of oligomeric E3 ubiquitin ligases
    • Vander Kooi CW,Ohi MD,Rosenberg JA, et al.The Prp19 U-box crystal structure suggests a common dimeric architecture for a class of oligomeric E3 ubiquitin ligases.Biochemistry. 2006;45:121-30.
    • (2006) Biochemistry , vol.45 , pp. 121-130
    • Vander Kooi, C.W.1    Ohi, M.D.2    Rosenberg, J.A.3
  • 79
    • 77950579617 scopus 로고    scopus 로고
    • The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines
    • David Y,Ziv T,Admon A,Navon A.The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines.J Biol Chem. 2010;285:8595-604.
    • (2010) J Biol Chem , vol.285 , pp. 8595-8604
    • David, Y.1    Ziv, T.2    Admon, A.3    Navon, A.4
  • 80
    • 33644850903 scopus 로고    scopus 로고
    • A UbcH5/ubiquitin noncovalent complex is required for processive BRCA1-directed ubiquitination
    • Brzovic PS,Lissounov A,Christensen DE,Hoyt DW,Klevit RE.A UbcH5/ubiquitin noncovalent complex is required for processive BRCA1-directed ubiquitination.Mol Cell. 2006;21:873-80.
    • (2006) Mol Cell , vol.21 , pp. 873-880
    • Brzovic, P.S.1    Lissounov, A.2    Christensen, D.E.3    Hoyt, D.W.4    Klevit, R.E.5
  • 81
    • 33846239416 scopus 로고    scopus 로고
    • The Mdm2 RING domain C-terminus is required for supramolecular assembly and ubiquitin ligase activity
    • Poyurovsky MV,Priest C,Kentsis A, et al.The Mdm2 RING domain C-terminus is required for supramolecular assembly and ubiquitin ligase activity.EMBO J. 2007;26:90-101.
    • (2007) EMBO J , vol.26 , pp. 90-101
    • Poyurovsky, M.V.1    Priest, C.2    Kentsis, A.3
  • 82
    • 72449125109 scopus 로고    scopus 로고
    • ATM activates p53 by regulating MDM2 oligomerization and E3 processivity
    • Cheng Q,Chen L,Li Z,Lane WS,Chen J.ATM activates p53 by regulating MDM2 oligomerization and E3 processivity.EMBO J. 2009;28:3857-67.
    • (2009) EMBO J , vol.28 , pp. 3857-3867
    • Cheng, Q.1    Chen, L.2    Li, Z.3    Lane, W.S.4    Chen, J.5
  • 83
    • 33748920505 scopus 로고    scopus 로고
    • Solution structure of the Hdm2 C2H2C4 RING, a domain critical for ubiquitination of p53
    • Kostic M,Matt T,Martinez-Yamout MA,Dyson HJ,Wright PE.Solution structure of the Hdm2 C2H2C4 RING, a domain critical for ubiquitination of p53.J Mol Biol. 2006;363:433-50.
    • (2006) J Mol Biol , vol.363 , pp. 433-450
    • Kostic, M.1    Matt, T.2    Martinez-Yamout, M.A.3    Dyson, H.J.4    Wright, P.E.5
  • 85
    • 79952453180 scopus 로고    scopus 로고
    • UBE4B promotes Hdm2-mediated degradation of the tumor suppressor p53
    • Wu H,Pomeroy SL,Ferreira M, et al.UBE4B promotes Hdm2-mediated degradation of the tumor suppressor p53.Nat Med. 2011;17:347-55.
    • (2011) Nat Med , vol.17 , pp. 347-355
    • Wu, H.1    Pomeroy, S.L.2    Ferreira, M.3
  • 86
    • 1842421376 scopus 로고    scopus 로고
    • A dynamic role of HAUSP in the p53-Mdm2 pathway
    • Li M,Brooks CL,Kon N,Gu W.A dynamic role of HAUSP in the p53-Mdm2 pathway.Mol Cell. 2004;13:879-86.
    • (2004) Mol Cell , vol.13 , pp. 879-886
    • Li, M.1    Brooks, C.L.2    Kon, N.3    Gu, W.4
  • 88
    • 33746648187 scopus 로고    scopus 로고
    • Critical role for Daxx in regulating Mdm2
    • Tang J,Qu LK,Zhang J, et al.Critical role for Daxx in regulating Mdm2.Nat Cell Biol. 2006;8:855-62.
    • (2006) Nat Cell Biol , vol.8 , pp. 855-862
    • Tang, J.1    Qu, L.K.2    Zhang, J.3
  • 89
    • 0034729759 scopus 로고    scopus 로고
    • Unmasking of phosphorylation-sensitive epitopes on p53 and Mdm2 by a simple Western-phosphatase procedure
    • Maya R,Oren M.Unmasking of phosphorylation-sensitive epitopes on p53 and Mdm2 by a simple Western-phosphatase procedure.Oncogene. 2000;19:3213-5.
    • (2000) Oncogene , vol.19 , pp. 3213-3215
    • Maya, R.1    Oren, M.2
  • 90
    • 0034649503 scopus 로고    scopus 로고
    • ATM complexes with HDM2 and promotes its rapid phosphorylation in a p53-independent manner in normal and tumor human cells exposed to ionizing radiation
    • de Toledo SM,Azzam EI,Dahlberg WK,Gooding TB,Little JB.ATM complexes with HDM2 and promotes its rapid phosphorylation in a p53-independent manner in normal and tumor human cells exposed to ionizing radiation.Oncogene. 2000;19:6185-93.
    • (2000) Oncogene , vol.19 , pp. 6185-6193
    • de Toledo, S.M.1    Azzam, E.I.2    Dahlberg, W.K.3    Gooding, T.B.4    Little, J.B.5
  • 91
    • 79953665566 scopus 로고    scopus 로고
    • The phenotype of MDM2 auto-degradation after DNA damage is due to epitope masking by phosphorylation
    • Cheng Q,Chen J.The phenotype of MDM2 auto-degradation after DNA damage is due to epitope masking by phosphorylation.Cell Cycle. 2011;10:1162-6.
    • (2011) Cell Cycle , vol.10 , pp. 1162-1166
    • Cheng, Q.1    Chen, J.2
  • 92
    • 0030881590 scopus 로고    scopus 로고
    • Differential regulation of the p21/WAF-1 and Mdm2 genes after high-dose UV irradiation: p53-dependent and p53-independent regulation of the Mdm2 gene
    • Wu L,Levine AJ.Differential regulation of the p21/WAF-1 and Mdm2 genes after high-dose UV irradiation: p53-dependent and p53-independent regulation of the Mdm2 gene.Mol Med. 1997;3:441-51.
    • (1997) Mol Med , vol.3 , pp. 441-451
    • Wu, L.1    Levine, A.J.2
  • 93
    • 0036340096 scopus 로고    scopus 로고
    • Hypophosphorylation of Mdm2 augments p53 stability
    • Blattner C,Hay T,Meek DW,Lane DP.Hypophosphorylation of Mdm2 augments p53 stability.Mol Cell Biol. 2002;22:6170-82.
    • (2002) Mol Cell Biol , vol.22 , pp. 6170-6182
    • Blattner, C.1    Hay, T.2    Meek, D.W.3    Lane, D.P.4
  • 94
    • 11144328933 scopus 로고    scopus 로고
    • Protein kinase CK1delta phosphorylates key sites in the acidic domain of murine double-minute clone 2 protein (MDM2) that regulate p53 turnover
    • Winter M,Milne D,Dias S, et al.Protein kinase CK1delta phosphorylates key sites in the acidic domain of murine double-minute clone 2 protein (MDM2) that regulate p53 turnover.Biochemistry. 2004;43:16356-64.
    • (2004) Biochemistry , vol.43 , pp. 16356-16364
    • Winter, M.1    Milne, D.2    Dias, S.3
  • 95
    • 23344447873 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3-dependent phosphorylation of Mdm2 regulates p53 abundance
    • Kulikov R,Boehme KA,Blattner C.Glycogen synthase kinase 3-dependent phosphorylation of Mdm2 regulates p53 abundance.Mol Cell Biol. 2005;25:7170-80.
    • (2005) Mol Cell Biol , vol.25 , pp. 7170-7180
    • Kulikov, R.1    Boehme, K.A.2    Blattner, C.3
  • 96
    • 77955535107 scopus 로고    scopus 로고
    • Phosphorylation by casein kinase I promotes the turnover of the Mdm2 oncoprotein via the SCF(beta-TRCP) ubiquitin ligase
    • Inuzuka H,Tseng A,Gao D, et al.Phosphorylation by casein kinase I promotes the turnover of the Mdm2 oncoprotein via the SCF(beta-TRCP) ubiquitin ligase.Cancer Cell. 2010;18:147-59.
    • (2010) Cancer Cell , vol.18 , pp. 147-159
    • Inuzuka, H.1    Tseng, A.2    Gao, D.3
  • 98
    • 0037047345 scopus 로고    scopus 로고
    • The conformationally flexible S9-S10 linker region in the core domain of p53 contains a novel MDM2 binding site whose mutation increases ubiquitination of p53 in vivo
    • Shimizu H,Burch LR,Smith AJ, et al.The conformationally flexible S9-S10 linker region in the core domain of p53 contains a novel MDM2 binding site whose mutation increases ubiquitination of p53 in vivo.J Biol Chem. 2002;277:28446-58.
    • (2002) J Biol Chem , vol.277 , pp. 28446-28458
    • Shimizu, H.1    Burch, L.R.2    Smith, A.J.3
  • 99
    • 33749013398 scopus 로고    scopus 로고
    • Binding of p53 to the central domain of Mdm2 is regulated by phosphorylation
    • Kulikov R,Winter M,Blattner C.Binding of p53 to the central domain of Mdm2 is regulated by phosphorylation.J Biol Chem. 2006;281:28575-83.
    • (2006) J Biol Chem , vol.281 , pp. 28575-28583
    • Kulikov, R.1    Winter, M.2    Blattner, C.3
  • 102
    • 27144444111 scopus 로고    scopus 로고
    • ATM and Chk2-dependent phosphorylation of MDMX contribute to p53 activation after DNA damage
    • Chen L,Gilkes DM,Pan Y,Lane WS,Chen J.ATM and Chk2-dependent phosphorylation of MDMX contribute to p53 activation after DNA damage.EMBO J. 2005;24:3411-22.
    • (2005) EMBO J , vol.24 , pp. 3411-3422
    • Chen, L.1    Gilkes, D.M.2    Pan, Y.3    Lane, W.S.4    Chen, J.5
  • 103
    • 20144387944 scopus 로고    scopus 로고
    • Phosphorylation of Hdmx mediates its Hdm2- and ATM-dependent degradation in response to DNA damage
    • Pereg Y,Shkedy D,de Graaf P, et al.Phosphorylation of Hdmx mediates its Hdm2- and ATM-dependent degradation in response to DNA damage.Proc Natl Acad Sci U S A. 2005;102:5056-61.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 5056-5061
    • Pereg, Y.1    Shkedy, D.2    de Graaf, P.3
  • 104
    • 33645293151 scopus 로고    scopus 로고
    • 14-3-3gamma binds to MDMX that is phosphorylated by UV-activated Chk1, resulting in p53 activation
    • Jin Y,Dai MS,Lu SZ, et al.14-3-3gamma binds to MDMX that is phosphorylated by UV-activated Chk1, resulting in p53 activation.EMBO J. 2006;25:1207-18.
    • (2006) EMBO J , vol.25 , pp. 1207-1218
    • Jin, Y.1    Dai, M.S.2    Lu, S.Z.3
  • 105
    • 33645290219 scopus 로고    scopus 로고
    • Regulation of MDMX nuclear import and degradation by Chk2 and 14-3-3
    • LeBron C,Chen L,Gilkes DM,Chen J.Regulation of MDMX nuclear import and degradation by Chk2 and 14-3-3.EMBO J. 2006;25:1196-206.
    • (2006) EMBO J , vol.25 , pp. 1196-1206
    • LeBron, C.1    Chen, L.2    Gilkes, D.M.3    Chen, J.4
  • 106
    • 63649142709 scopus 로고    scopus 로고
    • c-Abl phosphorylates Hdmx and regulates its interaction with p53
    • Zuckerman V,Lenos K,Popowicz GM, et al.c-Abl phosphorylates Hdmx and regulates its interaction with p53.J Biol Chem. 2009;284:4031-9.
    • (2009) J Biol Chem , vol.284 , pp. 4031-4039
    • Zuckerman, V.1    Lenos, K.2    Popowicz, G.M.3
  • 107
    • 0035949588 scopus 로고    scopus 로고
    • A phosphatidylinositol 3-kinase/Akt pathway promotes translocation of Mdm2 from the cytoplasm to the nucleus
    • Mayo LD,Donner DB.A phosphatidylinositol 3-kinase/Akt pathway promotes translocation of Mdm2 from the cytoplasm to the nucleus.Proc Natl Acad Sci U S A. 2001;98:11598-603.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 11598-11603
    • Mayo, L.D.1    Donner, D.B.2
  • 108
    • 0035736487 scopus 로고    scopus 로고
    • HER-2/neu induces p53 ubiquitination via Akt-mediated MDM2 phosphorylation
    • Zhou BP,Liao Y,Xia W,Zou Y,Spohn B,Hung MC.HER-2/neu induces p53 ubiquitination via Akt-mediated MDM2 phosphorylation.Nat Cell Biol. 2001;3:973-82.
    • (2001) Nat Cell Biol , vol.3 , pp. 973-982
    • Zhou, B.P.1    Liao, Y.2    Xia, W.3    Zou, Y.4    Spohn, B.5    Hung, M.C.6
  • 109
    • 7544247852 scopus 로고    scopus 로고
    • A novel site of AKT-mediated phosphorylation in the human MDM2 onco-protein
    • Milne D,Kampanis P,Nicol S, et al.A novel site of AKT-mediated phosphorylation in the human MDM2 onco-protein.FEBS Lett. 2004;577:270-6.
    • (2004) FEBS Lett , vol.577 , pp. 270-276
    • Milne, D.1    Kampanis, P.2    Nicol, S.3
  • 110
  • 111
    • 0036837868 scopus 로고    scopus 로고
    • DNA damage induces MDMX nuclear translocation by p53-dependent and -independent mechanisms
    • Li C,Chen L,Chen J.DNA damage induces MDMX nuclear translocation by p53-dependent and -independent mechanisms.Mol Cell Biol. 2002;22:7562-71.
    • (2002) Mol Cell Biol , vol.22 , pp. 7562-7571
    • Li, C.1    Chen, L.2    Chen, J.3
  • 112
    • 0036510399 scopus 로고    scopus 로고
    • Hdmx recruitment into the nucleus by Hdm2 is essential for its ability to regulate p53 stability and transactivation
    • Migliorini D,Danovi D,Colombo E,Carbone R,Pelicci PG,Marine JC.Hdmx recruitment into the nucleus by Hdm2 is essential for its ability to regulate p53 stability and transactivation.J Biol Chem. 2002;277:7318-23.
    • (2002) J Biol Chem , vol.277 , pp. 7318-7323
    • Migliorini, D.1    Danovi, D.2    Colombo, E.3    Carbone, R.4    Pelicci, P.G.5    Marine, J.C.6
  • 113
    • 27144541490 scopus 로고    scopus 로고
    • DNA damage-induced phosphorylation of MdmX at serine 367 activates p53 by targeting MdmX for Mdm2-dependent degradation
    • Okamoto K,Kashima K,Pereg Y, et al.DNA damage-induced phosphorylation of MdmX at serine 367 activates p53 by targeting MdmX for Mdm2-dependent degradation.Mol Cell Biol. 2005;25:9608-20.
    • (2005) Mol Cell Biol , vol.25 , pp. 9608-9620
    • Okamoto, K.1    Kashima, K.2    Pereg, Y.3
  • 114
    • 70350223615 scopus 로고    scopus 로고
    • Phosphorylation and degradation of MdmX is inhibited by Wip1 phosphatase in the DNA damage response
    • Zhang X,Lin L,Guo H, et al.Phosphorylation and degradation of MdmX is inhibited by Wip1 phosphatase in the DNA damage response.Cancer Res. 2009;69:7960-8.
    • (2009) Cancer Res , vol.69 , pp. 7960-7968
    • Zhang, X.1    Lin, L.2    Guo, H.3
  • 115
    • 78650963650 scopus 로고    scopus 로고
    • c-Abl phosphorylation of Mdm2 facilitates Mdm2-Mdmx complex formation
    • Waning DL,Lehman JA,Batuello CN,Mayo LD.c-Abl phosphorylation of Mdm2 facilitates Mdm2-Mdmx complex formation.J Biol Chem. 2011;286:216-22.
    • (2011) J Biol Chem , vol.286 , pp. 216-222
    • Waning, D.L.1    Lehman, J.A.2    Batuello, C.N.3    Mayo, L.D.4
  • 116
    • 19444367393 scopus 로고    scopus 로고
    • Loss of HAUSP-mediated deubiquitination contributes to DNA damage-induced destabilization of Hdmx and Hdm2
    • Meulmeester E,Maurice MM,Boutell C, et al.Loss of HAUSP-mediated deubiquitination contributes to DNA damage-induced destabilization of Hdmx and Hdm2.Mol Cell. 2005;18:565-76.
    • (2005) Mol Cell , vol.18 , pp. 565-576
    • Meulmeester, E.1    Maurice, M.M.2    Boutell, C.3
  • 117
    • 33748636939 scopus 로고    scopus 로고
    • Differential roles of ATM- and Chk2-mediated phosphorylations of Hdmx in response to DNA damage
    • Pereg Y,Lam S,Teunisse A, et al.Differential roles of ATM- and Chk2-mediated phosphorylations of Hdmx in response to DNA damage.Mol Cell Biol. 2006;26:6819-31.
    • (2006) Mol Cell Biol , vol.26 , pp. 6819-6831
    • Pereg, Y.1    Lam, S.2    Teunisse, A.3
  • 118
    • 67649361514 scopus 로고    scopus 로고
    • Increased radioresistance and accelerated B cell lymphomas in mice with Mdmx mutations that prevent modifications by DNA-damage-activated kinases
    • Wang YV,Leblanc M,Wade M,Jochemsen AG,Wahl GM.Increased radioresistance and accelerated B cell lymphomas in mice with Mdmx mutations that prevent modifications by DNA-damage-activated kinases.Cancer Cell. 2009;16:33-43.
    • (2009) Cancer Cell , vol.16 , pp. 33-43
    • Wang, Y.V.1    Leblanc, M.2    Wade, M.3    Jochemsen, A.G.4    Wahl, G.M.5
  • 119
    • 22544438112 scopus 로고    scopus 로고
    • Regulation of p53-MDMX interaction by casein kinase 1 alpha
    • Chen L,Li C,Pan Y,Chen J.Regulation of p53-MDMX interaction by casein kinase 1 alpha.Mol Cell Biol. 2005;25:6509-20.
    • (2005) Mol Cell Biol , vol.25 , pp. 6509-6520
    • Chen, L.1    Li, C.2    Pan, Y.3    Chen, J.4
  • 120
    • 13844294211 scopus 로고    scopus 로고
    • The casein kinase 1 family: participation in multiple cellular processes in eukaryotes
    • Knippschild U,Gocht A,Wolff S,Huber N,Lohler J,Stoter M.The casein kinase 1 family: participation in multiple cellular processes in eukaryotes.Cell Signal. 2005;17:675-89.
    • (2005) Cell Signal , vol.17 , pp. 675-689
    • Knippschild, U.1    Gocht, A.2    Wolff, S.3    Huber, N.4    Lohler, J.5    Stoter, M.6
  • 121
    • 79951784529 scopus 로고    scopus 로고
    • CKIalpha ablation highlights a critical role for p53 in invasiveness control
    • Elyada E,Pribluda A,Goldstein RE, et al.CKIalpha ablation highlights a critical role for p53 in invasiveness control.Nature. 2011;470:409-13.
    • (2011) Nature , vol.470 , pp. 409-413
    • Elyada, E.1    Pribluda, A.2    Goldstein, R.E.3
  • 122
    • 84864910054 scopus 로고    scopus 로고
    • Abnormal MDMX degradation in tumor cells due to ARF deficiency
    • Li X,Gilkes D,Li B, et al.Abnormal MDMX degradation in tumor cells due to ARF deficiency.Oncogene. 2011;:.
    • (2011) Oncogene
    • Li, X.1    Gilkes, D.2    Li, B.3
  • 124
    • 66449094959 scopus 로고    scopus 로고
    • A function for the RING finger domain in the allosteric control of MDM2 conformation and activity
    • Wawrzynow B,Pettersson S,Zylicz A, et al.A function for the RING finger domain in the allosteric control of MDM2 conformation and activity.J Biol Chem. 2009;284:11517-30.
    • (2009) J Biol Chem , vol.284 , pp. 11517-11530
    • Wawrzynow, B.1    Pettersson, S.2    Zylicz, A.3
  • 126
    • 77952387813 scopus 로고    scopus 로고
    • Phosphorylation-induced conformational changes in the retinoblastoma protein inhibit E2F transactivation domain binding
    • Burke JR,Deshong AJ,Pelton JG,Rubin SM.Phosphorylation-induced conformational changes in the retinoblastoma protein inhibit E2F transactivation domain binding.J Biol Chem. 2010;285:16286-93.
    • (2010) J Biol Chem , vol.285 , pp. 16286-16293
    • Burke, J.R.1    Deshong, A.J.2    Pelton, J.G.3    Rubin, S.M.4


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